作者: Akiyoshi TANAKA , Hayuki SUGIMOTO , Yuko MUTA , Takafumi MIZUNO , Keishi SENOO
DOI: 10.1271/BBB.67.207
关键词:
摘要: Thermal unfolding of P. cepacia lipase was observed by adiabatic differential scanning microcalorimetry in the absence and presence calcium ions at pH 8, thermodynamic parameters were evaluated to analyze mechanism enzyme. The temperature higher concentrations Ca2+. From Ca2+ concentration-dependence temperature, number that dissociated from enzyme molecule upon estimated be one. These results confirmed validity proposed previously: NCa2+↔D+Ca2+, where N D represent native denatured states, respectively,